- NSF awards $22.5 million to capture biology at the atomic level using X-ray lasers
- BioXFEL Research Support Call for Proposals
- UWM researchers create first 3D movie of virus in action
- Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature
- Protein structure determination using metagenome sequence data
- Thursday, 05 October 2017
On October 4th, 2017, Drs. Jacques Dubochet (formerly of University of Lausanne in Switzerland), Joachim Frank (Columbia University), and Richard Henderson (British Medical Research Council’s Laboratory of Molecular Biology in Cambridge, UK) were awarded the Nobel Prize in Chemistry for developing cryo-electron microscopy (Cryo-EM) for the high resolution structure determination of biomolecules in solution.
- Tuesday, 12 September 2017
Scientists who make movies of molecules in motion have a new high-speed camera to shoot with. The €1.2-billion (US$1.4-billion) European X-ray Free Electron Laser (XFEL) will start running its first experiments in September near Hamburg, Germany. The European XFEL fires powerful X-rays in bursts of a few hundred femtoseconds: so short that, like strobe lights, they can capture snapshots of jittery molecules frozen in time, and with a wavelength small enough to provide pictures at atomic resolution.
- Tuesday, 29 August 2017
Mix-and-inject serial crystallography (MISC) is a technique designed to image enzyme catalyzed reactions in which small protein crystals are mixed with a substrate just prior to being probed by an X-ray pulse. This approach offers several advantages over flow cell studies. It provides (i) room temperature structures at near atomic resolution, (ii) time resolution ranging from microseconds to seconds, and (iii) convenient reaction initiation.
- Thursday, 24 August 2017
BioXFEL researcher Peter Schwander released a publication, along with his peers, to Nature Methods
Using a manifold-based analysis of experimental diffraction snapshots from an X-ray free electron laser, we determine the three-dimensional structure and conformational landscape of the PR772 virus to a detector-limited resolution of 9 nm. Our results indicate that a single conformational coordinate controls reorganization of the genome, growth of a tubular structure from a portal vertex and release of the genome.
- Monday, 14 August 2017
A research collaboration led by the University of Wisconsin-Milwaukee has for the first time created a three-dimensional movie showing a virus preparing to infect a healthy cell.
The research has the potential to fundamentally advance our understanding of how biological processes inside the cell work. That could lead to better treatment for the horde of human diseases caused by viruses.
The feat was made possible by UWM physicists, who developed a new generation of powerful algorithms to reconstruct sequential images from an ocean of unsorted, noisy data.
- Thursday, 10 August 2017
BioXFEL scientist Vadim Cherezov and his colleagues released a new publication to CellPress:
X-ray free electron lasers (XFELs) have the potential to revolutionize macromolecular structural biology due to the unique combination of spatial coherence, extreme peak brilliance, and short duration of X-ray pulses. A recently emerged serial femtosecond (fs) crystallography (SFX) approach using XFEL radiation overcomes some of the biggest hurdles of traditional crystallography related to radiation damage through the diffraction-before-destruction principle.
- Experimental strategies for imaging bioparticles with femtosecond hard X-ray pulses
- Single-shot determination of focused FEL wave fields using iterative phase retrieval
- Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase
- Structural insights into the extracellular recognition of the human serotonin 2B receptor by an antibody
- FELIX: an algorithm for indexing multiple crystallites in X-ray free-electron laser snapshot diffraction images